Nitrogen-fixing Klebsiella species produce indole-3-acetic acid
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چکیده
منابع مشابه
Aromatic amino acid aminotransferase activity and indole-3-acetic acid production by associative nitrogen-fixing bacteria.
In this work, we report the detection of aromatic amino acid aminotransferase (AAT) activity from cell-free crude extracts of nine strains of N(2)-fixing bacteria from three genera. Using tyrosine as substrate, AAT activity ranged in specific activity from 0.084 to 0.404 micromol min(-1)mg(-1). When analyzed under non-denaturating PAGE conditions; and using tryptophan, phenylalanine, tyrosine, ...
متن کاملIndole-3-Acetic Acid and Flowering.
Science, a weekly journal, Is published each Friday by the American Association for the Advancement of Science at The Business Press, Incorporated, N. Queen St. and McGovern Ave., Lancaster, P'a. Founded In 1880. it has been since 1900 the official publication of the AAAS. Editorial and Advertising Offices, 1515 Massachusetts Avenue, N.W.. Washington 5, D. C. Telephone, EXecutive 80 or 661. Cab...
متن کاملRecent advances in nitrogen-fixing acetic acid bacteria.
Nitrogen is an essential plant nutrient, widely applied as N-fertilizer to improve yield of agriculturally important crops. An interesting alternative to avoid or reduce the use of N-fertilizers could be the exploitation of plant growth-promoting bacteria (PGPB), capable of enhancing growth and yield of many plant species, several of agronomic and ecological significance. PGPB belong to diverse...
متن کاملOxindole-3-acetic Acid, an Indole-3-acetic Acid Catabolite in Zea mays.
A prior study (13) from this laboratory showed that oxidation of exogenously applied indole-3-acetic acid (IAA) to oxindole-3-acetic acid (OxIAA) is the major catabolic pathway for IAA in Zea mays endosperm. In this work, we demonstrate that OxIAA is a naturally occurring compound in shoot and endosperm tissue of Z. mays and that the amount of OxIAA in both shoot and endosperm tissue is approxi...
متن کاملThe Nitrilase ZmNIT2 converts indole-3-acetonitrile to indole-3-acetic acid.
We isolated two nitrilase genes, ZmNIT1 and ZmNIT2, from maize (Zea mays) that share 75% sequence identity on the amino acid level. Despite the relatively high homology to Arabidopsis NIT4, ZmNIT2 shows no activity toward beta-cyano-alanine, the substrate of Arabidopsis NIT4, but instead hydrolyzes indole-3-acetonitrile (IAN) to indole-3-acetic acid (IAA). ZmNIT2 converts IAN to IAA at least se...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 1990
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.0002a8